slr1641 | ATP-dependent chaperone clpB
AS08 344 | Clonality: Polyclonal | Host: Rabbit | Reactivity: Cyanobacteria
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recombinant clpB1 protein, derived from Synechocystis PCC 6803 strain slr1641 sequence; protein has an internal translation site. The nomenclature used is reverse of what is mentioned in the cyanobase.
98.1 | 85.4 and 105 | 95 kDa for Synechocystis
10 μg of total protein from Synechocystis PCC 6803 wild type (+ClpB1) and slr1641 deletion mutant, control (C) and heat shocked samples (HS) was separated on 8% PAA gel and blotted on nitrocellulose membrane . Filters were blocked (1h), incubated with 1: 3000 anti-ClpB1 antibodies (2h) followed by incubation with 1: 2500 secondary anti-rabbit (1h) coupled to HRP and visualization with chemiluminescent detection reagent.
Courtesy of Dr. Elizabeth Vierling, University of Massachusetts, USA
ClpB protein is essential for resistance to high temperature stress. It functions to dissolve inactive protein aggregates that accumulate at high temperatures. Giese and Vierling (2002) Changes in oligomerization are essential for the chaperone activity of a small heat shock protein in vivo and in vitro. J Biol Chem; 277(48): 46310-8.